Low level chemiluminescence of the cytochrome <i>c</i>‐catalyzed decomposition of hydrogen peroxide

Cadenas, Enrique; Varsavsky, Alicia I.; Boveris, A; Chance, Britton

doi:10.1016/0014-5793(80)80577-1

Cited by 23 publications

(8 citation statements)

References 17 publications

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“…The lethality of plumbagin for washed cells of L. plantarum only when oxygen and a carbon and energy source was present argues for the effect being due to a toxic product of oxygen reduction. Although Mn(II) has been clearly shown here and elsewhere to effectively scavenge 02, reports exist in the literature of Mn apparently scavenging both singlet oxygen (6) and the hydroxyl radical (10,11), as well as increasing the resistance of spores to heat and ionizing radiation (1,2).…”

Section: Discussionmentioning

confidence: 69%

Manganese and Defenses against Oxygen Toxicity in Lactobacillus plantarum

1981

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Lactobacillus plantarum is aerotolerant during log-phase growth on glucose, but is an obligate aerobe on polyols. Respiration was cyanide resistant and under certain conditions was associated with the accumulation of millimolar concentrations of H202. On glucose, optimal growth was observed in the absence of 02. Extracts of L. plantarum did not catalyze the reduction of paraquat by reduced nicotinamide adenine dinucleotide, but plumbagin (5-hydroxy-2-methyl-1,4naphthoquinone) was readily reduced. Such extracts produced O2 in the presence of NADH plus plumbagin. Plumbagin caused a 10-fold increase in the rate of respiration of intact cells in the presence of glucose and also imposed a loss of viability which was dependent upon both glucose and 02. Although extracts of L. plantarum were devoid of true superoxide dismutase activity, this organisim was comparable to superoxide dismutase-containing species in its resistance toward hyperbaric 02 and toward the oxygen-dependent lethality of plumbagin. L. plantarum required Mn-rich media and actively accumulated Mn(II). Soluble extracts were found to contain approximately 9 jig of Mn per mg of protein and 75 to 90% of this Mn was dialyzable. Such extracts exhibited a dialyzable and ethylenediaminetetraacetic acid-inhibitable ability to scavenge 02. This 02scavenging activity was due to the dialyzable Mn(ll) present in these extracts and could be mimicked by MnCl2. Cells grown in Mn-rich media were enriched in dialyzable Mn and were more resistant toward oxygen toxicity and toward the oxygen-dependent plumbagin toxicity than were cells grown in Mn-deficient media. L. plantarum exhibited no nutritional requirement for iron and little or no iron was present in these cells, even when they were grown in iron-rich media. L.

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Section: Discussionmentioning

confidence: 69%

Manganese and Defenses against Oxygen Toxicity in Lactobacillus plantarum

1981

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“…On the other hand, the possible generation of singlet oxygen through a peroxidase-catalysed decomposition of malonaldehyde (Vidigal-Martinelli et al, 1979) seems very unlikely to occur in the present conditions; although liver homogenate might provide a peroxidase activity necessary to these reactions, its strict requirement of Mn2+ would halt the reaction. Moreover, we have reported on the inhibitory effect of Mn2+ on chemiluminescence (Cadenas et al, 1980f).…”

Section: Rh+ho"-h20+r"mentioning

confidence: 99%

Oxygen- or organic hydroperoxide-induced chemiluminescence of brain and liver homogenates

Cadenas¹,

Varsavsky²,

Boveris³

et al. 1981

Biochemical Journal

105

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Oxygenation of anaerobically isolated brain and liver homogenates is associated with chemiluminescence and formation of lipid hydroperoxides, the latter determined by the thiobarbituric acid assay. Light emission and formation of malonaldehyde are 20-fold higher in the brain than in liver; chemiluminescence of both decays when accumulation of malonaldehyde ceases. Exogenous organic peroxides, such as t-butyl hydroperoxide, inhibit the light-emission response to oxygenation by brain homogenate, whereas they enhance that of liver homogenate. t-Butyl hydroperoxide-induced photoemission of liver homogenate shows a polyphasic kinetic pattern that is O2-dependent. The spectral analysis of chemiluminescence arising from brain and liver homogenates on oxygenation shows a spectrum with five emission bands at 420-450, 475-485, 510-540, 560-580 and 625-640 nm. These bands are subjected to intensity changes or shifts of the wavelength whenever t-butyl hydroperoxide is present, either inhibiting or stimulating light emission. The blue-band chemiluminescence, around 435 nm, is possibly due to the weak light emission arising from excited carbonyl compounds [Lloyd (1965) J. Chem. Soc. Faraday Trans. 61, 2182-2193; Vassil'ev (1965) Opt. Spectrosc. (USSR) 18, 131-135], whereas the presence of other bands suggests generation of singlet molecular oxygen either in the process triggered on oxygenation (lipid oxygenation) or after supplementation with organic hydroperoxides. We offer several explanations for the spectral analysis presented here.

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“…Specifically, we have shown that GSH and DCFH 2 compete for oxidation by the same oxidizing species. Although the ability of the cyt c/H 2 O 2 couple to initiate biomolecular oxidation has been known for several years, the identity of the oxidizing species has not been established (50,51,(63)(64)(65). Several workers have considered formation of the hydroxyl radical through redox cycling (50,51,63), involving the initial reduction of the ferricytochrome by either superoxide or hydrogen peroxide (Reactions 2-4).…”

Section: Traces B and D)mentioning

confidence: 99%

Evidence for the Role of a Peroxidase Compound I-type Intermediate in the Oxidation of Glutathione, NADH, Ascorbate, and Dichlorofluorescin by Cytochrome c/H2O2

Lawrence

Jones

Wardman

et al. 2003

Journal of Biological Chemistry

160

106

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The release of cytochrome c from mitochondria is a crucial step in apoptosis, resulting in the activation of the caspase proteases. A further consequence of cytochrome c release is the enhanced mitochondrial production of superoxide radicals (O 2 . ), which are converted to hydrogen peroxide by manganese-superoxide dismutase. Recently, we showed that cytochrome c is a potent catalyst of 2,7-dichlorofluorescin oxidation to the fluorescent 2,7-dichlorofluorescein by these species, leading to the conclusion that 2,7-dichlorofluorescein fluorescence is a reflection of cytosolic cytochrome c concentration rather than "reactive oxygen species" levels (Burkitt, M. J., and Wardman, P.

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Low level chemiluminescence of the cytochrome c‐catalyzed decomposition of hydrogen peroxide

Cited by 23 publications

References 17 publications

Manganese and Defenses against Oxygen Toxicity in Lactobacillus plantarum

Manganese and Defenses against Oxygen Toxicity in Lactobacillus plantarum

Oxygen- or organic hydroperoxide-induced chemiluminescence of brain and liver homogenates

Evidence for the Role of a Peroxidase Compound I-type Intermediate in the Oxidation of Glutathione, NADH, Ascorbate, and Dichlorofluorescin by Cytochrome c/H2O2

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